Growth of giant two-dimensional crystal of protein molecules from a three-phase contact line.
A novel method to fabricate a two-dimensional (2D) crystal of protein molecules has been developed. The method enables us to control both the position of nucleation and the direction of the crystal growth. The crystal obtained using a protein molecule, ferritin, was found to be composed of a number of densely packed single crystal domains with an unprecedentedly large size of approximately 100 microm(2). This method also reveals characteristic behavior of the spatiotemporal evolution of the crystal; for example, "fusion" of the crystal domains, which is never observed in an ordinary crystal composed of atoms or ions, was demonstrated. Our approach could have potential in fabricating extraordinarily large and highly ordered nanoparticle arrays of organic or inorganic materials.
Ikezoe
Yasuhiro
Y
Flucto-Order Functions Asian Collaboration Team, RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. y.ikezoe@riken.jp
Kumashiro
Yoshikazu
Y
Tamada
Kaoru
K
Matsui
Takuro
T
Yamashita
Ichiro
I
Shiba
Kiyotaka
K
Hara
Masahiko
M
D002021:Buffers; D002627:Chemistry, Physical / Q000379:methods; D003460:Crystallization; D005293:Ferritins / Q000737:chemistry; D005583:Fourier Analysis; D006863:Hydrogen-Ion Concentration; D008855:Microscopy, Electron, Scanning; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D013997:Time Factors; D014965:X-Rays
D002021:Buffers; D011506:Proteins; D005293:Ferritins